| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSD17b12 |
| Uniprot No | Q53GQ0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-312aa |
| 氨基酸序列 | MESALPAAGFLYWVGAGTVAYLALRISYSLFTALRVWGVGNEAGVGPGLGEWAVVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASEDIYDKIKTGLAGLEIGILVNNVGMSYEYPEYFLDVPDLDNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKPSPETFVKSAIKTVGLQSRTNGYLIHALMGSIISNLPSWIYLKIVMNMNKSTRAHYLKKTKKN |
| 预测分子量 | 34,3 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于HSD17β12重组蛋白的模拟参考文献示例(文献信息为虚构，仅供格式参考)：
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1. **文献名称**: *Cloning and Functional Characterization of Human HSD17B12 Recombinant Protein*
**作者**: Smith A, et al.
**摘要**: 本研究成功在大肠杆菌中表达并纯化了HSD17β12重组蛋白，验证了其17β-羟类固醇脱氢酶活性，证实其对雌二醇/雌酮转化的催化作用，并发现该酶对长链脂肪酸代谢的可能影响。
2. **文献名称**: *Structural Insights into HSD17B12 through Recombinant Expression and Crystallography*
**作者**: Chen L, et al.
**摘要**: 通过昆虫细胞表达系统获得高纯度HSD17β12重组蛋白，解析其晶体结构，揭示底物结合域的关键氨基酸残基，为靶向药物设计提供结构基础。
3. **文献名称**: *HSD17B12 Recombinant Protein in Lipid Metabolism: Role in Stearoyl-CoA Desaturase Regulation*
**作者**: Tanaka K, et al.
**摘要**: 利用哺乳动物细胞表达重组HSD17β12.证明其通过调节硬脂酰辅酶A去饱和酶(SCD1)活性参与脂肪酸去饱和过程，提示其在脂代谢疾病中的潜在作用。
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**注意**：以上文献为模拟内容，实际研究中请通过PubMed、Google Scholar等平台检索真实文献(关键词：HSD17B12 recombinant expression/kinetics/lipid metabolism)。
**Background of HSD17B12 Recombinant Protein**
HSD17B12 (17β-hydroxysteroid dehydrogenase type 12) is a member of the 17β-HSD enzyme family, which plays a critical role in steroidogenesis and lipid metabolism. This endoplasmic reticulum-associated protein catalyzes the reduction of 17-keto-steroids to 17β-hydroxysteroids, a key step in synthesizing active steroid hormones like estradiol and testosterone. Beyond steroids, HSD17B12 is integral to fatty acid elongation as part of the fatty acid synthase complex, converting 3-ketoacyl-CoA intermediates to 3-hydroxyacyl-CoA during long-chain fatty acid synthesis.
Recombinant HSD17B12 protein is engineered using expression systems (e.g., *E. coli*, mammalian cells) to produce purified, functional enzyme for research. Its recombinant form retains catalytic activity, enabling studies on substrate specificity, enzyme kinetics, and interaction partners. Researchers utilize this protein to explore its dual metabolic roles, particularly its involvement in hormone-dependent cancers (e.g., breast, prostate) where dysregulated HSD17B12 expression correlates with tumor progression and therapy resistance.
Structural studies of recombinant HSD17B12 have identified conserved Rossmann-fold domains characteristic of short-chain dehydrogenases/reductases (SDRs), along with cofactor-binding regions for NADPH/NADH. These insights aid in designing inhibitors targeting its steroidogenic or lipid metabolic functions. Additionally, the protein serves as an antigen for antibody development, supporting diagnostic and therapeutic applications.
HSD17B12’s involvement in critical metabolic pathways underscores its potential as a biomarker or drug target. Research using recombinant variants continues to clarify its physiological and pathological roles, bridging gaps in understanding endocrine regulation, lipid homeostasis, and cancer biology.
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